1idd

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[[Image:1idd.jpg|left|200px]]
 
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==ISOCITRATE DEHYDROGENASE Y160F MUTANT APO ENZYME==
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The line below this paragraph, containing "STRUCTURE_1idd", creates the "Structure Box" on the page.
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<StructureSection load='1idd' size='340' side='right'caption='[[1idd]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1idd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IDD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IDD FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1idd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1idd OCA], [https://pdbe.org/1idd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1idd RCSB], [https://www.ebi.ac.uk/pdbsum/1idd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1idd ProSAT]</span></td></tr>
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{{STRUCTURE_1idd| PDB=1idd | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/IDH_ECOLI IDH_ECOLI]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/id/1idd_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1idd ConSurf].
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<div style="clear:both"></div>
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'''ISOCITRATE DEHYDROGENASE Y160F MUTANT APO ENZYME'''
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==See Also==
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*[[Isocitrate dehydrogenase 3D structures|Isocitrate dehydrogenase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Two site-directed mutants of isocitrate dehydrogenase (IDH) of Escherichia coli have been studied by site-directed mutagenesis kinetic and structural studies. Substitution of phenylalanine for tyrosine at position 160 (Y160F) showed 0.4% of the kcat of wild-type with isocitrate as substrate, while the Km for isocitrate remained unchanged. When the postulated intermediate, oxalosuccinate, was enzymatically decarboxylated, Y160F showed a higher kcat and a similar Km to the wild type values. The rate of reduction of oxalosuccinate to isocitrate by the Y160F mutant was greatly decreased relative to the wild-type. Substitution of methionine for lysine at position 230 decreased kcat to 1.1% of that of the wild-type and Km increased by a factor of 500-600. The decarboxylation of oxalosuccinate was undetectable for the K230M mutant. The structure of the site-directed mutants of IDH with and without a bound complex of isocitrate and Mg2+ was solved at 2.5 A resolution and compared by difference mapping against previously determined enzyme structures. The structural studies show that (i) the overall protein-folding side chain conformations and active sites of both mutants are isomorphous with wild-type enzyme, (ii) isocitrate and magnesium bind to both enzyme mutants with the same relative conformation and binding interactions as wild-type enzyme, and (iii) the mutated side chains (Phe 160 and Met 230) are positioned for catalysis in a similar conformation as that observed for the wild-type enzyme. Hence, the alteration of the side chain functional groups is directly related to the loss of enzyme activity. Possible roles of the active site tyrosine and lysine are discussed.
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==About this Structure==
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1IDD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IDD OCA].
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==Reference==
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Mutational analysis of the catalytic residues lysine 230 and tyrosine 160 in the NADP(+)-dependent isocitrate dehydrogenase from Escherichia coli., Lee ME, Dyer DH, Klein OD, Bolduc JM, Stoddard BL, Koshland DE Jr, Biochemistry. 1995 Jan 10;34(1):378-84. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7819221 7819221]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Bolduc, J M.]]
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[[Category: Bolduc JM]]
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[[Category: Dyer, D H.]]
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[[Category: Dyer DH]]
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[[Category: Junior, D E.Koshland.]]
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[[Category: Klein OD]]
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[[Category: Klein, O D.]]
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[[Category: Koshland Junior DE]]
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[[Category: Lee, M E.]]
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[[Category: Lee ME]]
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[[Category: Stoddard, B L.]]
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[[Category: Stoddard BL]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:52:23 2008''
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Current revision

ISOCITRATE DEHYDROGENASE Y160F MUTANT APO ENZYME

PDB ID 1idd

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